4FLE

Crystal structure of the esterase YqiA (YE3661) from Yersinia enterocolitica, Northeast Structural Genomics Consortium Target YeR85

PDB DOI: https://doi.org/10.2210/pdb4FLE/pdb

Classification: HYDROLASE
Organism(s): Yersinia enterocolitica subsp. enterocolitica 8081
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2012-06-14 Released: 2012-08-08
Deposition Author(s): Forouhar, F., Lew, S., Seetharaman, J., Shastry, R., Kohan, E., Maglaqui, M., Mao, L., Xiao, R., Acton, T.B., Everett, J.K., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium, Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.249
R-Value Work: 0.194
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Crystal structure of the esterase YqiA (YE3661) from Yersinia enterocolitica, Northeast Structural Genomics Consortium Target YeR85 (CASP Target)

Forouhar, F., Lew, S., Seetharaman, J., Shastry, R., Kohan, E., Maglaqui, M., Mao, L., Xiao, R., Acton, T.B., Everett, J.K., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium

To be published.

Macromolecule Content

Total Structure Weight: 23.08 kDa
Atom Count: 1,726
Modelled Residue Count: 195
Deposited Residue Count: 202
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
esterase	A	202	Yersinia enterocolitica subsp. enterocolitica 8081	Mutation(s): 0 Gene Names: YE3661
UniProt
Find proteins for A1JQU0 (Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)) Explore A1JQU0 Go to UniProtKB: A1JQU0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	A1JQU0
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.249
R-Value Work: 0.194
R-Value Observed: 0.194
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 55.056	α = 90
b = 79.543	β = 90
c = 46.06	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
ADSC	data collection
DENZO	data reduction
SCALEPACK	data scaling
SHELXS	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2012-08-08

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2012-08-08
Type: Initial release
Version 1.1: 2017-10-25
Changes: Author supporting evidence

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.